|Title||Function of rhodopsin in temperature discrimination in Drosophila|
|Publication Type||Journal Article|
|Year of Publication||2011|
|Authors||Shen WL, Kwon Y, Adegbola AA, Luo J, Chess A, Montell C|
|Date Published||2011 Mar 11|
|Keywords||Animals, Drosophila melanogaster, Drosophila Proteins, Eye Proteins, Larva, Light, Mice, Movement, Mutation, Photoreceptor Cells, Invertebrate, Receptors, G-Protein-Coupled, Rhodopsin, Rod Opsins, Signal Transduction, Temperature, Thermosensing, TRPC Cation Channels|
Many animals, including the fruit fly, are sensitive to small differences in ambient temperature. The ability of Drosophila larvae to choose their ideal temperature (18°C) over other comfortable temperatures (19° to 24°C) depends on a thermosensory signaling pathway that includes a heterotrimeric guanine nucleotide-binding protein (G protein), a phospholipase C, and the transient receptor potential TRPA1 channel. We report that mutation of the gene (ninaE) encoding a classical G protein-coupled receptor (GPCR), Drosophila rhodopsin, eliminates thermotactic discrimination in the comfortable temperature range. This role for rhodopsin in thermotaxis toward 18°C was light-independent. Introduction of mouse melanopsin restored normal thermotactic behavior in ninaE mutant larvae. We propose that rhodopsins represent a class of evolutionarily conserved GPCRs that are required for initiating thermosensory signaling cascades.
|Grant List||GM085335 / GM / NIGMS NIH HHS / United States|